메뉴 건너뛰기




Volumn 421, Issue 2, 2011, Pages 141-148

The mechanism of DNA ejection in the Bacillus anthracis spore-binding phage 8a revealed by cryo-electron tomography

Author keywords

Bacillus anthracis; Bacteriophage; Base plate; Contractile tail; Cryo electron tomography; DNA ejection; Myoviridae; Phage infection; Tail contraction; Tail sheath

Indexed keywords

BACTERIOPHAGE DNA; CAPSID PROTEIN; SPORE BINDING PHAGE 8A; UNCLASSIFIED DRUG;

EID: 80455122642     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2011.08.028     Document Type: Article
Times cited : (20)

References (55)
  • 2
    • 75849141082 scopus 로고    scopus 로고
    • Gp15 and gp16 cooperate in translocating bacteriophage T7 DNA into the infected cell
    • Chang C.Y., Kemp P., Molineux I.J. Gp15 and gp16 cooperate in translocating bacteriophage T7 DNA into the infected cell. Virology 2010, 398:176-186.
    • (2010) Virology , vol.398 , pp. 176-186
    • Chang, C.Y.1    Kemp, P.2    Molineux, I.J.3
  • 3
    • 42249109989 scopus 로고    scopus 로고
    • Insight into DNA and protein transport in double-stranded DNA viruses: the structure of bacteriophage N4
    • Choi K.H., McPartland J., Kaganman I., Bowman V.D., Rothman-Denes L.B., Rossmann M.G. Insight into DNA and protein transport in double-stranded DNA viruses: the structure of bacteriophage N4. J. Mol. Biol. 2008, 378:726-736.
    • (2008) J. Mol. Biol. , vol.378 , pp. 726-736
    • Choi, K.H.1    McPartland, J.2    Kaganman, I.3    Bowman, V.D.4    Rothman-Denes, L.B.5    Rossmann, M.G.6
  • 4
    • 14744274379 scopus 로고    scopus 로고
    • DNA ejection from bacteriophage T5: analysis of the kinetics and energetics
    • de Frutos M., Letellier L., Raspaud E. DNA ejection from bacteriophage T5: analysis of the kinetics and energetics. Biophys. J. 2005, 88:1364-1370.
    • (2005) Biophys. J. , vol.88 , pp. 1364-1370
    • de Frutos, M.1    Letellier, L.2    Raspaud, E.3
  • 6
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy 2000, 85:225-234.
    • (2000) Ultramicroscopy , vol.85 , pp. 225-234
    • Egelman, E.H.1
  • 10
    • 16344390563 scopus 로고    scopus 로고
    • Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography
    • Forster F., Medalia O., et al. Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography. Proc. Natl. Acad. Sci. U. S. A. 2005, 102(13):4729-4734.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.13 , pp. 4729-4734
    • Forster, F.1    Medalia, O.2
  • 11
    • 35548972992 scopus 로고    scopus 로고
    • Real-time observations of single bacteriophage [U+4F4D] DNA ejections in vitro
    • Grayson P., Han L., Winther T., Phillips R. Real-time observations of single bacteriophage [U+4F4D] DNA ejections in vitro. Proc. Natl. Acad. Sci. 2007, 104:14652-14657.
    • (2007) Proc. Natl. Acad. Sci. , vol.104 , pp. 14652-14657
    • Grayson, P.1    Han, L.2    Winther, T.3    Phillips, R.4
  • 12
    • 0032516784 scopus 로고    scopus 로고
    • Crystallographic analysis reveals the 12-fold symmetry of the bacteriophage [phi]29 connector particle
    • Guasch A., Pous J., Praga A., Valpuesta J.M., Carrascosa J.L., Coll M. Crystallographic analysis reveals the 12-fold symmetry of the bacteriophage [phi]29 connector particle. J. Mol. Biol. 1998, 281:219-225.
    • (1998) J. Mol. Biol. , vol.281 , pp. 219-225
    • Guasch, A.1    Pous, J.2    Praga, A.3    Valpuesta, J.M.4    Carrascosa, J.L.5    Coll, M.6
  • 13
    • 33745714419 scopus 로고    scopus 로고
    • Dynamics of DNA ejection from bacteriophage
    • Inamdar M.M., Gelbart W.M., Phillips R. Dynamics of DNA ejection from bacteriophage. Biophys. J. 2006, 91:411-420.
    • (2006) Biophys. J. , vol.91 , pp. 411-420
    • Inamdar, M.M.1    Gelbart, W.M.2    Phillips, R.3
  • 14
    • 31844435708 scopus 로고    scopus 로고
    • Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus
    • Jiang W., Chang J., Jakana J., Weigele P., King J., Chiu W. Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus. Nature 2006, 439:612-616.
    • (2006) Nature , vol.439 , pp. 612-616
    • Jiang, W.1    Chang, J.2    Jakana, J.3    Weigele, P.4    King, J.5    Chiu, W.6
  • 16
    • 4344657166 scopus 로고    scopus 로고
    • Bacteriophage T7 DNA ejection into cells is initiated by an enzyme-like mechanism
    • Kemp P., Gupta M., Molineux I.J. Bacteriophage T7 DNA ejection into cells is initiated by an enzyme-like mechanism. Mol. Microbiol. 2004, 53:1251-1265.
    • (2004) Mol. Microbiol. , vol.53 , pp. 1251-1265
    • Kemp, P.1    Gupta, M.2    Molineux, I.J.3
  • 17
    • 24944579983 scopus 로고    scopus 로고
    • Changes in bacteriophage T7 virion structure at the initiation of infection
    • Kemp P., Garcia L.R., Molineux I.J. Changes in bacteriophage T7 virion structure at the initiation of infection. Virology 2005, 340:307-317.
    • (2005) Virology , vol.340 , pp. 307-317
    • Kemp, P.1    Garcia, L.R.2    Molineux, I.J.3
  • 19
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer J.R., Mastronarde D.N., McIntosh J.R. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 1996, 116:71-76.
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 22
    • 4644242580 scopus 로고    scopus 로고
    • Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host
    • Leiman P.G., Chipman P.R., Kostyuchenko V.A., Mesyanzhinov V.V., Rossmann M.G. Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host. Cell 2004, 118:419-429.
    • (2004) Cell , vol.118 , pp. 419-429
    • Leiman, P.G.1    Chipman, P.R.2    Kostyuchenko, V.A.3    Mesyanzhinov, V.V.4    Rossmann, M.G.5
  • 23
    • 33748286733 scopus 로고    scopus 로고
    • Electron tomography of swollen rigor fibers of insect flight muscle reveals a short and variably angled S2 domain
    • Liu J., Wu S., Reedy M.C., Winkler H., Lucaveche C., Cheng Y., Reedy M.K., Taylor K.A. Electron tomography of swollen rigor fibers of insect flight muscle reveals a short and variably angled S2 domain. J. Mol. Biol. 2006, 362:844-860.
    • (2006) J. Mol. Biol. , vol.362 , pp. 844-860
    • Liu, J.1    Wu, S.2    Reedy, M.C.3    Winkler, H.4    Lucaveche, C.5    Cheng, Y.6    Reedy, M.K.7    Taylor, K.A.8
  • 25
    • 67749093018 scopus 로고    scopus 로고
    • Intact flagellar motor of Borrelia burgdorferi revealed by cryo-electron tomography: evidence for stator ring curvature and rotor/C ring assembly flexion
    • Liu J., Lin T., Botkin D.J., McCrum E., Winkler H., Norris S.J. Intact flagellar motor of Borrelia burgdorferi revealed by cryo-electron tomography: evidence for stator ring curvature and rotor/C ring assembly flexion. J. Bacteriol. 2009, 16:5026-5036.
    • (2009) J. Bacteriol. , vol.16 , pp. 5026-5036
    • Liu, J.1    Lin, T.2    Botkin, D.J.3    McCrum, E.4    Winkler, H.5    Norris, S.J.6
  • 26
    • 77957266487 scopus 로고    scopus 로고
    • 3D visualization of HIV virions by cryoelectron tomography
    • Liu J., Wright E.R., et al. 3D visualization of HIV virions by cryoelectron tomography. Methods Enzymol. 2010, 483:267-290.
    • (2010) Methods Enzymol. , vol.483 , pp. 267-290
    • Liu, J.1    Wright, E.R.2
  • 27
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: from cells to molecules
    • Lucic V., Forster F., Baumeister W. Structural studies by electron tomography: from cells to molecules. Annu. Rev. Biochem. 2005, 74:833-865.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 833-865
    • Lucic, V.1    Forster, F.2    Baumeister, W.3
  • 28
    • 16244387909 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space
    • Matias V.R., Beveridge T.J. Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space. Mol. Microbiol. 2005, 56:240-251.
    • (2005) Mol. Microbiol. , vol.56 , pp. 240-251
    • Matias, V.R.1    Beveridge, T.J.2
  • 29
    • 0037044862 scopus 로고    scopus 로고
    • Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography
    • Medalia O., Weber I., Frangakis A.S., Nicastro D., Gerisch G., Baumeister W. Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography. Science 2002, 298:1209-1213.
    • (2002) Science , vol.298 , pp. 1209-1213
    • Medalia, O.1    Weber, I.2    Frangakis, A.S.3    Nicastro, D.4    Gerisch, G.5    Baumeister, W.6
  • 30
    • 0014219440 scopus 로고
    • Structure of the sheath of bacteriophage T4 I. Structure of the contracted sheath and polysheath
    • Moody M.F. Structure of the sheath of bacteriophage T4 I. Structure of the contracted sheath and polysheath. J. Mol. Biol. 1967, 25:167-174.
    • (1967) J. Mol. Biol. , vol.25 , pp. 167-174
    • Moody, M.F.1
  • 31
    • 0014219345 scopus 로고
    • Structure of the sheath of bacteriophage T4 II. Rearrangement of the sheath subunits during contraction
    • Moody M.F. Structure of the sheath of bacteriophage T4 II. Rearrangement of the sheath subunits during contraction. J. Mol. Biol. 1967, 25:201-202.
    • (1967) J. Mol. Biol. , vol.25 , pp. 201-202
    • Moody, M.F.1
  • 32
    • 0015867079 scopus 로고
    • Sheath of bacteriophage T4: III. Contraction mechanism deduced from partially contracted sheaths
    • Moody M.F. Sheath of bacteriophage T4: III. Contraction mechanism deduced from partially contracted sheaths. J. Mol. Biol. 1973, 80:613-620.
    • (1973) J. Mol. Biol. , vol.80 , pp. 613-620
    • Moody, M.F.1
  • 34
    • 17044395121 scopus 로고    scopus 로고
    • Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of [phi]29
    • Morais M.C., Choi K.H., Koti J.S., Chipman P.R., Anderson D.L., Rossmann M.G. Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of [phi]29. Mol. Cell 2005, 18:149-159.
    • (2005) Mol. Cell , vol.18 , pp. 149-159
    • Morais, M.C.1    Choi, K.H.2    Koti, J.S.3    Chipman, P.R.4    Anderson, D.L.5    Rossmann, M.G.6
  • 35
    • 17044395121 scopus 로고    scopus 로고
    • Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of phi29
    • Morais M.C., Choi K.H., Koti J.S., Chipman P.R., Anderson D.L., Rossmann M.G. Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of phi29. Mol. Cell 2005, 18:149-159.
    • (2005) Mol. Cell , vol.18 , pp. 149-159
    • Morais, M.C.1    Choi, K.H.2    Koti, J.S.3    Chipman, P.R.4    Anderson, D.L.5    Rossmann, M.G.6
  • 36
    • 0027981449 scopus 로고
    • Structural and physicochemical analysis of the contractile MM phage tail and comparison with the bacteriophage T4 tail
    • Müler M., Engel A., Aebi U. Structural and physicochemical analysis of the contractile MM phage tail and comparison with the bacteriophage T4 tail. J. Struct. Biol. 1994, 112:11-31.
    • (1994) J. Struct. Biol. , vol.112 , pp. 11-31
    • Müler, M.1    Engel, A.2    Aebi, U.3
  • 37
    • 0343811707 scopus 로고    scopus 로고
    • The bacteriophage [phgr]29 head-tail connector imaged at high resolution with the atomic force microscope in buffer solution
    • Muller D.J., Engel A., Carrascosa J.L., Velez M. The bacteriophage [phgr]29 head-tail connector imaged at high resolution with the atomic force microscope in buffer solution. EMBO J. 1997, 16:2547-2553.
    • (1997) EMBO J. , vol.16 , pp. 2547-2553
    • Muller, D.J.1    Engel, A.2    Carrascosa, J.L.3    Velez, M.4
  • 41
    • 70349971642 scopus 로고    scopus 로고
    • Phage-mediated bioluminescent detection of Bacillus anthracis
    • Schofield D.A., Westwater C. Phage-mediated bioluminescent detection of Bacillus anthracis. J. Appl. Microbiol. 2009, 107:1468-1478.
    • (2009) J. Appl. Microbiol. , vol.107 , pp. 1468-1478
    • Schofield, D.A.1    Westwater, C.2
  • 42
    • 71549137749 scopus 로고    scopus 로고
    • Diagnostic bioluminescent phage for detection of Yersinia pestis
    • Schofield D.A., Molineux I.J., Westwater C. Diagnostic bioluminescent phage for detection of Yersinia pestis. J. Clin. Microbiol. 2009, 47:3887-3894.
    • (2009) J. Clin. Microbiol. , vol.47 , pp. 3887-3894
    • Schofield, D.A.1    Molineux, I.J.2    Westwater, C.3
  • 45
    • 2542491187 scopus 로고    scopus 로고
    • Mapping of functional sites on the primary structure of the contractile tail sheath protein of bacteriophage T4 by mutation analysis
    • Takeda S., Suzuki M., Yamada T., Kageyama M., Arisaka F. Mapping of functional sites on the primary structure of the contractile tail sheath protein of bacteriophage T4 by mutation analysis. Biochim. Biophys. Acta, Proteins Proteomics 2004, 1699:163-171.
    • (2004) Biochim. Biophys. Acta, Proteins Proteomics , vol.1699 , pp. 163-171
    • Takeda, S.1    Suzuki, M.2    Yamada, T.3    Kageyama, M.4    Arisaka, F.5
  • 47
    • 0032582665 scopus 로고    scopus 로고
    • Assembly of a tailed bacterial virus and its genome release studied in three dimensions
    • Tao Y., Olson N.H., Xu W., Anderson D.L., Rossmann M.G., Baker T.S. Assembly of a tailed bacterial virus and its genome release studied in three dimensions. Cell 1998, 95:431-437.
    • (1998) Cell , vol.95 , pp. 431-437
    • Tao, Y.1    Olson, N.H.2    Xu, W.3    Anderson, D.L.4    Rossmann, M.G.5    Baker, T.S.6
  • 48
    • 0036424944 scopus 로고    scopus 로고
    • A novel three-dimensional variant of the watershed transform for segmentation of electron density maps
    • Volkmann N. A novel three-dimensional variant of the watershed transform for segmentation of electron density maps. J. Struct. Biol. 2002, 138:123-129.
    • (2002) J. Struct. Biol. , vol.138 , pp. 123-129
    • Volkmann, N.1
  • 49
    • 0038677491 scopus 로고    scopus 로고
    • Efficacy and durability of Bacillus anthracis bacteriophages used against spores
    • Walter M.H. Efficacy and durability of Bacillus anthracis bacteriophages used against spores. J. Environ. Heal. 2003, 66.
    • (2003) J. Environ. Heal. , vol.66
    • Walter, M.H.1
  • 50
    • 0038500847 scopus 로고    scopus 로고
    • Three Bacillus anthracis bacteriophages from topsoil
    • Walter M.H., Baker D.D. Three Bacillus anthracis bacteriophages from topsoil. Curr. Microbiol. 2003, 47:55-58.
    • (2003) Curr. Microbiol. , vol.47 , pp. 55-58
    • Walter, M.H.1    Baker, D.D.2
  • 52
    • 33845310367 scopus 로고    scopus 로고
    • 3D reconstruction and processing of volumetric data in cryo-electron tomography
    • Winkler H. 3D reconstruction and processing of volumetric data in cryo-electron tomography. J. Struct. Biol. 2007, 157:126-137.
    • (2007) J. Struct. Biol. , vol.157 , pp. 126-137
    • Winkler, H.1
  • 53
    • 29244462551 scopus 로고    scopus 로고
    • Accurate marker-free alignment with simultaneous geometry determination and reconstruction of tilt series in electron tomography
    • Winkler H., Taylor K.A. Accurate marker-free alignment with simultaneous geometry determination and reconstruction of tilt series in electron tomography. Ultramicroscopy 2006, 106:240-254.
    • (2006) Ultramicroscopy , vol.106 , pp. 240-254
    • Winkler, H.1    Taylor, K.A.2
  • 54
    • 58349085125 scopus 로고    scopus 로고
    • Tomographic subvolume alignment and subvolume classification applied to myosin V and SIV envelope spikes
    • Winkler H., Zhu P., et al. Tomographic subvolume alignment and subvolume classification applied to myosin V and SIV envelope spikes. J. Struct. Biol. 2009, 165(2):64-77.
    • (2009) J. Struct. Biol. , vol.165 , Issue.2 , pp. 64-77
    • Winkler, H.1    Zhu, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.